Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects
Identifieur interne : 000994 ( Istex/Corpus ); précédent : 000993; suivant : 000995Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects
Auteurs : A. Bikfalvi ; C. Sauzeau ; H. Moukadiri ; J. Maclouf ; N. Busso ; M. Bryckaert ; J. Plouet ; G. TobelemSource :
- Journal of Cellular Physiology [ 0021-9541 ] ; 1991-10.
English descriptors
- Teeft :
- Acad, Acidic, Acidic wash, Activator, Amino acids, Angiogenesis, Angiogenic, Assay, Basic fibroblast growth factor, Bfgf, Bikfalvi, Binding sites, Biol, Bovine, Bovine capillary, Cell biol, Cell growth factor, Cell surface binding, Chloroquine, Collagen type, Connolly, Degradation, Degraded, Endothelial, Endothelial cell mitogen, Endothelial cells, Fibroblast, Gospodarowicz, Growth factor, Growth factors, Heparin, Human umbilical vein, Huve, Huve cells, Incubation medium, Inhibitor, Internalization, Ligand, Montesano, Moukadiri, Natl, Ngiml, Orci, Physiol, Plasminogen, Plasminogen activator, Plasminogen activators, Plouet, Proc, Procoagulant, Procoagulant activity, Prostacyclin, Prostacyclin production, Protamin, Radioactivity, Receptor, Tissue factor, Total radioactivity, Umbilical, Unlabeled, Unlabeled ligand, Unstimulated control, Vascular permeability factor, Vasculotropin, Vasculotropin effect, Vasi vegf, Vasivegf, Vegf.
Abstract
Vasculotropin/vascular endothelial cell growth factor (VAS/VEGF) is a newly purified growth factor with a unique specificity for vascular endothelial cells. We have investigated the interactions of VAS/VEGF with human umbilical vein endothelial cells (HUVE cells). 125I‐VAS/VEGF was bound to HUVE cells in a saturable manner with a half‐maximum binding at 2.8 ng/ml. Scatchard analysis did show two classes of high‐affinity binding sites. The first class displayed a dissociation constant of 9 pM with 500 sites/cell. The dissociation constant and the number of binding sites of the second binding class were variable for different HUVE cell cultures (KD = 179 ± 101 pM, 5,850 ± 2,950 sites/cell). Half‐maximal inhibition of 125I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with 125I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced 125I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. 125I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of 125I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. The angiogenic activity seems to be independent of the plasminogen activator or inhibitor system.
Url:
DOI: 10.1002/jcp.1041490108
Links to Exploration step
ISTEX:D65D97CC8479F9BF9489CDDB588AF8E067E434AALe document en format XML
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Bikfalvi</name><affiliation><mods:affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Current Address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York, NY 10076</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York, NY 10076</mods:affiliation></affiliation></author><author><name sortKey="Sauzeau, C" sort="Sauzeau, C" uniqKey="Sauzeau C" first="C." last="Sauzeau">C. Sauzeau</name><affiliation><mods:affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</mods:affiliation></affiliation></author><author><name sortKey="Moukadiri, H" sort="Moukadiri, H" uniqKey="Moukadiri H" first="H." last="Moukadiri">H. Moukadiri</name><affiliation><mods:affiliation>INSERM U 86, Centre des Cordeliers, 75006 Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse, France</mods:affiliation></affiliation></author><author><name sortKey="Maclouf, J" sort="Maclouf, J" uniqKey="Maclouf J" first="J." last="Maclouf">J. Maclouf</name><affiliation><mods:affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</mods:affiliation></affiliation></author><author><name sortKey="Busso, N" sort="Busso, N" uniqKey="Busso N" first="N." last="Busso">N. Busso</name><affiliation><mods:affiliation>Laboratoires Glaxo, 91940 Les Ulis, France</mods:affiliation></affiliation></author><author><name sortKey="Bryckaert, M" sort="Bryckaert, M" uniqKey="Bryckaert M" first="M." last="Bryckaert">M. Bryckaert</name><affiliation><mods:affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</mods:affiliation></affiliation></author><author><name sortKey="Plouet, J" sort="Plouet, J" uniqKey="Plouet J" first="J." last="Plouet">J. Plouet</name><affiliation><mods:affiliation>INSERM U 86, Centre des Cordeliers, 75006 Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse, France</mods:affiliation></affiliation></author><author><name sortKey="Tobelem, G" sort="Tobelem, G" uniqKey="Tobelem G" first="G." last="Tobelem">G. Tobelem</name><affiliation><mods:affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Cellular Physiology</title><title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title><idno type="ISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><imprint><biblScope unit="vol">149</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="50">50</biblScope><biblScope unit="page" to="59">59</biblScope><biblScope unit="page-count">10</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1991-10">1991-10</date></imprint><idno type="ISSN">0021-9541</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9541</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Acidic</term><term>Acidic wash</term><term>Activator</term><term>Amino acids</term><term>Angiogenesis</term><term>Angiogenic</term><term>Assay</term><term>Basic fibroblast growth factor</term><term>Bfgf</term><term>Bikfalvi</term><term>Binding sites</term><term>Biol</term><term>Bovine</term><term>Bovine capillary</term><term>Cell biol</term><term>Cell growth factor</term><term>Cell surface binding</term><term>Chloroquine</term><term>Collagen type</term><term>Connolly</term><term>Degradation</term><term>Degraded</term><term>Endothelial</term><term>Endothelial cell mitogen</term><term>Endothelial cells</term><term>Fibroblast</term><term>Gospodarowicz</term><term>Growth factor</term><term>Growth factors</term><term>Heparin</term><term>Human umbilical vein</term><term>Huve</term><term>Huve cells</term><term>Incubation medium</term><term>Inhibitor</term><term>Internalization</term><term>Ligand</term><term>Montesano</term><term>Moukadiri</term><term>Natl</term><term>Ngiml</term><term>Orci</term><term>Physiol</term><term>Plasminogen</term><term>Plasminogen activator</term><term>Plasminogen activators</term><term>Plouet</term><term>Proc</term><term>Procoagulant</term><term>Procoagulant activity</term><term>Prostacyclin</term><term>Prostacyclin production</term><term>Protamin</term><term>Radioactivity</term><term>Receptor</term><term>Tissue factor</term><term>Total radioactivity</term><term>Umbilical</term><term>Unlabeled</term><term>Unlabeled ligand</term><term>Unstimulated control</term><term>Vascular permeability factor</term><term>Vasculotropin</term><term>Vasculotropin effect</term><term>Vasi vegf</term><term>Vasivegf</term><term>Vegf</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Vasculotropin/vascular endothelial cell growth factor (VAS/VEGF) is a newly purified growth factor with a unique specificity for vascular endothelial cells. We have investigated the interactions of VAS/VEGF with human umbilical vein endothelial cells (HUVE cells). 125I‐VAS/VEGF was bound to HUVE cells in a saturable manner with a half‐maximum binding at 2.8 ng/ml. Scatchard analysis did show two classes of high‐affinity binding sites. The first class displayed a dissociation constant of 9 pM with 500 sites/cell. The dissociation constant and the number of binding sites of the second binding class were variable for different HUVE cell cultures (KD = 179 ± 101 pM, 5,850 ± 2,950 sites/cell). Half‐maximal inhibition of 125I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with 125I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced 125I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. 125I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of 125I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. The angiogenic activity seems to be independent of the plasminogen activator or inhibitor system.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>vasivegf</json:string><json:string>huve</json:string><json:string>huve cells</json:string><json:string>plasminogen</json:string><json:string>activator</json:string><json:string>angiogenesis</json:string><json:string>prostacyclin</json:string><json:string>bfgf</json:string><json:string>ngiml</json:string><json:string>angiogenic</json:string><json:string>montesano</json:string><json:string>fibroblast</json:string><json:string>receptor</json:string><json:string>internalization</json:string><json:string>prostacyclin production</json:string><json:string>growth factor</json:string><json:string>plouet</json:string><json:string>basic fibroblast growth factor</json:string><json:string>biol</json:string><json:string>orci</json:string><json:string>endothelial cells</json:string><json:string>binding sites</json:string><json:string>chloroquine</json:string><json:string>endothelial</json:string><json:string>bikfalvi</json:string><json:string>natl</json:string><json:string>unlabeled</json:string><json:string>acad</json:string><json:string>vegf</json:string><json:string>heparin</json:string><json:string>umbilical</json:string><json:string>moukadiri</json:string><json:string>total radioactivity</json:string><json:string>vasculotropin</json:string><json:string>proc</json:string><json:string>physiol</json:string><json:string>plasminogen activator</json:string><json:string>procoagulant</json:string><json:string>protamin</json:string><json:string>gospodarowicz</json:string><json:string>growth factors</json:string><json:string>human umbilical vein</json:string><json:string>cell growth factor</json:string><json:string>acidic</json:string><json:string>procoagulant activity</json:string><json:string>unlabeled ligand</json:string><json:string>radioactivity</json:string><json:string>assay</json:string><json:string>ligand</json:string><json:string>plasminogen activators</json:string><json:string>acidic wash</json:string><json:string>cell biol</json:string><json:string>vasculotropin effect</json:string><json:string>bovine capillary</json:string><json:string>collagen type</json:string><json:string>amino acids</json:string><json:string>endothelial cell mitogen</json:string><json:string>tissue factor</json:string><json:string>vasi vegf</json:string><json:string>degradation</json:string><json:string>connolly</json:string><json:string>degraded</json:string><json:string>bovine</json:string><json:string>inhibitor</json:string><json:string>incubation medium</json:string><json:string>unstimulated control</json:string><json:string>cell surface binding</json:string><json:string>vascular permeability factor</json:string></teeft></keywords><author><json:item><name>A. Bikfalvi</name><affiliations><json:string>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</json:string><json:string>Current Address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York, NY 10076</json:string><json:string>Correspondence address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York, NY 10076</json:string></affiliations></json:item><json:item><name>C. Sauzeau</name><affiliations><json:string>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</json:string></affiliations></json:item><json:item><name>H. Moukadiri</name><affiliations><json:string>INSERM U 86, Centre des Cordeliers, 75006 Paris, France</json:string><json:string>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse, France</json:string></affiliations></json:item><json:item><name>J. Maclouf</name><affiliations><json:string>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</json:string></affiliations></json:item><json:item><name>N. Busso</name><affiliations><json:string>Laboratoires Glaxo, 91940 Les Ulis, France</json:string></affiliations></json:item><json:item><name>M. Bryckaert</name><affiliations><json:string>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</json:string></affiliations></json:item><json:item><name>J. Plouet</name><affiliations><json:string>INSERM U 86, Centre des Cordeliers, 75006 Paris, France</json:string><json:string>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse, France</json:string></affiliations></json:item><json:item><name>G. Tobelem</name><affiliations><json:string>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</json:string></affiliations></json:item></author><articleId><json:string>JCP1041490108</json:string></articleId><arkIstex>ark:/67375/WNG-CDHTF6T2-B</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Vasculotropin/vascular endothelial cell growth factor (VAS/VEGF) is a newly purified growth factor with a unique specificity for vascular endothelial cells. We have investigated the interactions of VAS/VEGF with human umbilical vein endothelial cells (HUVE cells). 125I‐VAS/VEGF was bound to HUVE cells in a saturable manner with a half‐maximum binding at 2.8 ng/ml. Scatchard analysis did show two classes of high‐affinity binding sites. The first class displayed a dissociation constant of 9 pM with 500 sites/cell. The dissociation constant and the number of binding sites of the second binding class were variable for different HUVE cell cultures (KD = 179 ± 101 pM, 5,850 ± 2,950 sites/cell). Half‐maximal inhibition of 125I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with 125I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced 125I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. 125I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of 125I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. The angiogenic activity seems to be independent of the plasminogen activator or inhibitor system.</abstract><qualityIndicators><score>10</score><pdfWordCount>6585</pdfWordCount><pdfCharCount>41524</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>594 x 792 pts</pdfPageSize><pdfWordsPerPage>659</pdfWordsPerPage><pdfText>true</pdfText><refBibsNative>true</refBibsNative><abstractWordCount>285</abstractWordCount><abstractCharCount>2046</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects</title><pmid><json:string>1719003</json:string></pmid><genre><json:string>article</json:string></genre><host><title>Journal of Cellular Physiology</title><language><json:string>unknown</json:string></language><doi><json:string>10.1002/(ISSN)1097-4652</json:string></doi><issn><json:string>0021-9541</json:string></issn><eissn><json:string>1097-4652</json:string></eissn><publisherId><json:string>JCP</json:string></publisherId><volume>149</volume><issue>1</issue><pages><first>50</first><last>59</last><total>10</total></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Article</value></json:item><json:item><value>Articles</value></json:item></subject></host><namedEntities><unitex><date><json:string>1991</json:string><json:string>1251</json:string></date><geogName></geogName><orgName><json:string>Mobay Inc.</json:string><json:string>Pharmacia</json:string><json:string>Research</json:string><json:string>LISS, INC</json:string><json:string>American Diagnostica</json:string><json:string>Department of Cell Biology, New York University Medical Center</json:string><json:string>Biochem</json:string><json:string>American Diagnostica, Greenwich, CT</json:string><json:string>Rad</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>P.M. Henson</json:string><json:string>J. Plouet</json:string><json:string>J. Biol</json:string><json:string>J. Cell</json:string><json:string>J. Abraham</json:string><json:string>NY Acad</json:string><json:string>J. Exp</json:string><json:string>B. Murphy</json:string><json:string>J. Natl</json:string><json:string>J. Clin</json:string><json:string>D. Hicks</json:string></persName><placeName><json:string>Bedford</json:string><json:string>Uppsala</json:string><json:string>Paris</json:string><json:string>Greenwich</json:string><json:string>NY</json:string><json:string>Richmond</json:string><json:string>Mannheim</json:string><json:string>Kuwashima</json:string><json:string>Narbonne</json:string><json:string>VA</json:string><json:string>CT</json:string><json:string>Ferrara</json:string><json:string>Amsterdam</json:string><json:string>Toulouse</json:string><json:string>CA</json:string><json:string>MA</json:string><json:string>France</json:string><json:string>Sweden</json:string><json:string>Mountain View</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Plouet and Moukadiri, 1990a,b</json:string><json:string>Hasegawa et al., 1988</json:string><json:string>Pradelles et al., 1985</json:string><json:string>Bevilacqua et al., 1984, 1986</json:string><json:string>Moukadiri et al., 1990</json:string><json:string>Phillips et al. 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CELLS</title><author xml:id="author-0000" role="corresp"><persName><forename type="first">A.</forename><surname>Bikfalvi</surname></persName><affiliation><address><addrLine>INSERM U 150</addrLine><addrLine>Hopital Lariboisière, 75010 Paris, France</addrLine><country key="FR" xml:lang="en">FRANCE</country></address></affiliation><affiliation><orgName type="laboratory">Department of Cell Biology</orgName><orgName type="institution">New York University Medical Center</orgName><address><addrLine>550 First Avenue</addrLine><addrLine>New York, NY 10076</addrLine><country key="US" xml:lang="en">UNITED STATES</country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">C.</forename><surname>Sauzeau</surname></persName><affiliation><address><addrLine>INSERM U 150</addrLine><addrLine>Hopital Lariboisière, 75010 Paris, France</addrLine><country key="FR" xml:lang="en">FRANCE</country></address></affiliation></author><author 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Half‐maximal inhibition of <hi rend="superscript">125</hi>I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with <hi rend="superscript">125</hi>I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced <hi rend="superscript">125</hi>I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. <hi rend="superscript">125</hi>I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of <hi rend="superscript">125</hi>I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. 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We have investigated the interactions of VAS/VEGF with human umbilical vein endothelial cells (HUVE cells). <sup>125</sup>I‐VAS/VEGF was bound to HUVE cells in a saturable manner with a half‐maximum binding at 2.8 ng/ml. Scatchard analysis did show two classes of high‐affinity binding sites. The first class displayed a dissociation constant of 9 pM with 500 sites/cell. The dissociation constant and the number of binding sites of the second binding class were variable for different HUVE cell cultures (K<sub>D</sub> = 179 ± 101 pM, 5,850 ± 2,950 sites/cell). Half‐maximal inhibition of <sup>125</sup>I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with <sup>125</sup>I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced <sup>125</sup>I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. <sup>125</sup>I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of <sup>125</sup>I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. The angiogenic activity seems to be independent of the plasminogen activator or inhibitor system.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>VASCULOTROPIN EFFECT ON HUVE CELLS</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects</title></titleInfo><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Bikfalvi</namePart><affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</affiliation><affiliation>Current Address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York, NY 10076</affiliation><affiliation>Correspondence address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York, NY 10076</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C.</namePart><namePart type="family">Sauzeau</namePart><affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Moukadiri</namePart><affiliation>INSERM U 86, Centre des Cordeliers, 75006 Paris, France</affiliation><affiliation>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Maclouf</namePart><affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N.</namePart><namePart type="family">Busso</namePart><affiliation>Laboratoires Glaxo, 91940 Les Ulis, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Bryckaert</namePart><affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Plouet</namePart><affiliation>INSERM U 86, Centre des Cordeliers, 75006 Paris, France</affiliation><affiliation>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Tobelem</namePart><affiliation>INSERM U 150, Hopital Lariboisière, 75010 Paris, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">1991-10</dateIssued><dateCaptured encoding="w3cdtf">1991-03-05</dateCaptured><dateValid encoding="w3cdtf">1991-05-08</dateValid><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">7</extent><extent unit="tables">1</extent><extent unit="references">52</extent></physicalDescription><abstract lang="en">Vasculotropin/vascular endothelial cell growth factor (VAS/VEGF) is a newly purified growth factor with a unique specificity for vascular endothelial cells. We have investigated the interactions of VAS/VEGF with human umbilical vein endothelial cells (HUVE cells). 125I‐VAS/VEGF was bound to HUVE cells in a saturable manner with a half‐maximum binding at 2.8 ng/ml. Scatchard analysis did show two classes of high‐affinity binding sites. The first class displayed a dissociation constant of 9 pM with 500 sites/cell. The dissociation constant and the number of binding sites of the second binding class were variable for different HUVE cell cultures (KD = 179 ± 101 pM, 5,850 ± 2,950 sites/cell). Half‐maximal inhibition of 125I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with 125I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced 125I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. 125I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of 125I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. 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|texte= Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects
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